(data stored in SCRATCH zone)

SWISSPROT: KPYC_ARATH

ID   KPYC_ARATH              Reviewed;         497 AA.
AC   O65595;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   11-DEC-2019, entry version 148.
DE   RecName: Full=Probable pyruvate kinase, cytosolic isozyme;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   OrderedLocusNames=At4g26390; ORFNames=M3E9.180;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Key regulatory enzyme of the glycolytic pathway that
CC       catalyzes the final step of glycolysis, converting ADP and
CC       phosphoenolpyruvate (PEP) to ATP and pyruvate by essentially
CC       irreversible transphosphorylation. {ECO:0000250|UniProtKB:Q2RAK2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P30613}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q2RAK2}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
DR   EMBL; AL022223; CAA18231.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79494.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85192.1; -; Genomic_DNA.
DR   PIR; T05065; T05065.
DR   RefSeq; NP_194369.1; NM_118772.2.
DR   SMR; O65595; -.
DR   STRING; 3702.AT4G26390.1; -.
DR   PaxDb; O65595; -.
DR   PRIDE; O65595; -.
DR   EnsemblPlants; AT4G26390.1; AT4G26390.1; AT4G26390.
DR   GeneID; 828745; -.
DR   Gramene; AT4G26390.1; AT4G26390.1; AT4G26390.
DR   KEGG; ath:AT4G26390; -.
DR   Araport; AT4G26390; -.
DR   TAIR; locus:2131453; AT4G26390.
DR   eggNOG; KOG2323; Eukaryota.
DR   eggNOG; COG0469; LUCA.
DR   HOGENOM; HOG000021559; -.
DR   InParanoid; O65595; -.
DR   KO; K00873; -.
DR   OMA; DYLQCVI; -.
DR   OrthoDB; 933620at2759; -.
DR   PhylomeDB; O65595; -.
DR   BioCyc; ARA:AT4G26390-MONOMER; -.
DR   UniPathway; UPA00109; UER00188.
DR   PRO; PR:O65595; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65595; baseline and differential.
DR   Genevisible; O65595; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   Gene3D; 2.40.33.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.40.1380.20; -; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   PANTHER; PTHR11817; PTHR11817; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF50800; SSF50800; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52935; SSF52935; 1.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; O65595.
DR   SWISS-2DPAGE; O65595.
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..497
FT                   /note="Probable pyruvate kinase, cytosolic isozyme"
FT                   /id="PRO_0000112123"
FT   NP_BIND         39..42
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   METAL           39
FT                   /note="Potassium"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   METAL           41
FT                   /note="Potassium"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   METAL           71
FT                   /note="Potassium"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   METAL           72
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   METAL           229
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   METAL           253
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         37
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         78
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         163
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         227
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         252
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         253
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         285
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   SITE            227
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00549"
SQ   SEQUENCE   497 AA;  54319 MW;  45D43EF54A89FE62 CRC64;
     MAMEQRPKTK IVCTLGPASR SVPMVEKLLM AGMSVARFNF SHGSYEYHQE TLDNLRQAML
     NTGMLCAVML DTKGPEIRTG FLKDGKPIQL KQGQEITIST DYDLKGDEKT ICMSYKKLAQ
     DVNPGMVILC ADGTISLKVL SCDKEKGTVR CRCENTSMLG ERKNVNLPGV VVDLPTLTEK
     DKQDILEWGV PNQIDMIALS FVRKGSDLVQ VRKLLGKHAK TILLMSKVEN QEGVANFDDI
     LINSDAFMIA RGDLGMEIPI EKIFLAQKVM IYKCNFMGKP VVTATQMLES MIKSPRPTRA
     EATDVANAVL DGTDCVMLSG ETAAGAYPEL AVRTMAKICV EAESTLDYGD IFKRIMLHAA
     VPMSPMESLA SSAVRTATSS RATLMMVLTR GGSTARLVAK YRPGIPILSV VVPEITSDSF
     DWACSNEAPA RHSLIYRGLV PVLYAGSARA SIDESTEETL EFASEYGKKK QLCKTGDSVV
     ALFRTGNAIV IKILTVK
//

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